Immunodetection and photostability of NADPH-protochlorophyllide oxidoreductase in Pinus pinea L. |
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Authors: | Keli Ou Nicolle Packer Heather Adamson |
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Institution: | (1) School of Biological Science, Macquarie University, 2109 Sydney, N.S.W., Australia |
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Abstract: | Antibody against the light-dependent NADPH-protochlorophyllide oxidoreductase of oat was used to detect a protein of the same molecular weight in cotyledons of 40-day-old dark-grown seedlings of Pinus pinea L. Exposure of the seedlings to light resulted in a rapid decrease in protochlorophyllide content without the concomitant decrease in 38 kDa protein which is observed on transfer of dark-grown angiosperm seedlings to light. The stability of the light-dependent NADPH-protochlorophyllide oxidoreductase in pine in the absence of accumulated substrate is consistent with either (1) a different mechanism of regulation of chlorophyll synthesis in gymnosperms or (2) a higher proportion of stable extra-plastidic protein reacting with the antibody to the light-dependent NADPH-protochlorophyllide oxidoreductase than is the case in angiosperms.Abbreviations Chl
chlorophyll
- Chlide
chlorophyllide
- NADPH-Pchlide oxidoreductase
NADPH protochlorophyllide oxidoreductase
- NC
nitrocellulose
- PBS
phosphate buffered saline
- Pchlide
protochlorophyllide
- SDS
sodum dodecyl sulphate
- SDS-PAGE
sodium dodecyl sulphate polyacrylamide gel electrophoresis |
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Keywords: | NADPH-protochlorophyllide oxidoreductase protochlorophyllide light-grown dark-grown gymnosperm Pinus pinea |
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